Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2003-1-1
pubmed:abstractText
The Saccharomyces cerevisiae TOP3 gene encodes the type IA topoisomerase (Top3p) that is highly conserved in evolution. Deletion of TOP3 leads to a reduction in cell viability, hyper-recombination between repetitive DNA sequences, and abnormalities in both cell cycle progression and responses to DNA damaging agents. Deletion of SGS1, encoding the sole RecQ family helicase in S. cerevisiae, strongly suppresses the phenotypic effects of loss of TOP3 function. Here, we show that many of the adverse phenotypic effects of TOP3 deletion can also be partially alleviated by disruption of homologous recombination (HR) functions. This genetic interaction is seen both in strains deleted for TOP3 and in wild-type strains over-expressing a dominant-negative Top3p mutant form that confers a top3-like phenotype. Moreover, we show that this genetic interaction is conserved in the distantly-related fission yeast, Schizosaccharomyces pombe. Our results implicate topoisomerase III enzymes in recombination repair events required for cellular protection against DNA damaging agents and DNA replication inhibitors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases, http://linkedlifedata.com/resource/pubmed/chemical/DNA Topoisomerases, Type I, http://linkedlifedata.com/resource/pubmed/chemical/DNA topoisomerase III, http://linkedlifedata.com/resource/pubmed/chemical/Methyl Methanesulfonate, http://linkedlifedata.com/resource/pubmed/chemical/Mutagens, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/RAD53 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/RecQ Helicases, http://linkedlifedata.com/resource/pubmed/chemical/SGS1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1568-7864
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
463-82
pubmed:dateRevised
2008-12-25
pubmed:meshHeading
pubmed-meshheading:12509234-Blotting, Western, pubmed-meshheading:12509234-Cell Cycle, pubmed-meshheading:12509234-Cell Cycle Proteins, pubmed-meshheading:12509234-Cell Survival, pubmed-meshheading:12509234-DNA Damage, pubmed-meshheading:12509234-DNA Helicases, pubmed-meshheading:12509234-DNA Repair, pubmed-meshheading:12509234-DNA Topoisomerases, Type I, pubmed-meshheading:12509234-Epistasis, Genetic, pubmed-meshheading:12509234-Gene Expression Regulation, Fungal, pubmed-meshheading:12509234-Genes, Dominant, pubmed-meshheading:12509234-Humans, pubmed-meshheading:12509234-Methyl Methanesulfonate, pubmed-meshheading:12509234-Mutagenesis, pubmed-meshheading:12509234-Mutagens, pubmed-meshheading:12509234-Phenotype, pubmed-meshheading:12509234-Phosphorylation, pubmed-meshheading:12509234-Protein-Serine-Threonine Kinases, pubmed-meshheading:12509234-RecQ Helicases, pubmed-meshheading:12509234-Recombination, Genetic, pubmed-meshheading:12509234-Saccharomyces cerevisiae, pubmed-meshheading:12509234-Saccharomyces cerevisiae Proteins, pubmed-meshheading:12509234-Schizosaccharomyces, pubmed-meshheading:12509234-Sequence Deletion, pubmed-meshheading:12509234-Ultraviolet Rays
pubmed:year
2002
pubmed:articleTitle
Inactivation of homologous recombination suppresses defects in topoisomerase III-deficient mutants.
pubmed:affiliation
Cancer Research UK Laboratories, Weatherall Institute of Molecular Medicine, University of Oxford, John Radcliffe Hospital, Oxford OX3 9DS, UK.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't